Muscular laminopathies: Role of prelamin A in early steps of muscle differentiation

2011 ◽  
Vol 51 (1) ◽  
pp. 246-256 ◽  
Author(s):  
Nadir M. Maraldi ◽  
Cristina Capanni ◽  
Rosalba Del Coco ◽  
Stefano Squarzoni ◽  
Marta Columbaro ◽  
...  
Keyword(s):  
Muscle Differentiation ◽  
Prelamin A

Development of the iris in the chicken embryo

Development ◽  
1984 ◽  
Vol 81 (1) ◽  
pp. 169-183
Author(s):  
Patricia A. Ferrari ◽  
William E. Koch
Keyword(s):  
Epithelial Cells ◽  
Chicken Embryo ◽  
Muscle Differentiation ◽  
Muscle Fibres ◽  
Tissue Interactions ◽  
Morphological Organization ◽  
Chicken Muscle ◽  
Muscle Myosin

The developmental capabilities of the iris rudiment in the chicken embryo, as well as the role of tissue interactions in the differentiation of the iris, were investigated in vitro. Sectors of the intact iris from 7½- through 9-day embryos (stages 32 through 35) lost their morphological organization in vitro, but were capable of normal histodifferentiation. The pigmentation of the epithelium increased, and muscle differentiation occurred. Developing muscle was identified using immunocytochemistry with antiserum against chicken muscle myosin; this procedure permitted positive identification of myoblasts, myotubes, and muscle fibres in cultures in which histological features alone were equivocal. The proportion of irideal explants which developed muscle increased with the age of the embryo, and correlated with the incidence of epithelial buds and epithelial cells in the stroma. Irideal mesenchyme from stage-32 through stage-35 embryos was already populated with stromal epithelial cells when isolated, but growth and muscle differentiation in these cultures compared poorly with that in the intact iris in vitro. Isolated irideal epithelium (stages 32 through 37) demonstrated even more limited muscle differentiation in vitro, suggesting reciprocal interaction between irideal epithelium and mesenchyme during development. Irideal epithelium was also cultured in direct association with non-irideal mesenchyme from various embryonic organ rudiments, but muscle differentiation was not enhanced.

scholarly journals Insulin-Like Growth Factor Binding Protein-6 Promotes the Differentiation of Placental Mesenchymal Stem Cells into Skeletal Muscle Independent of Insulin-Like Growth Factor Receptor-1 and Insulin Receptor

2019 ◽  
Vol 2019 ◽  
pp. 1-18 ◽  
Author(s):  
Doaa Aboalola ◽  
Victor K. M. Han
Keyword(s):  
Skeletal Muscle ◽  
Stem Cells ◽  
Mesenchymal Stem Cells ◽  
Growth Factor ◽  
Muscle Differentiation ◽  
Insulin Like Growth Factor ◽  
Differentiation Process ◽  
Placental Mesenchymal Stem Cells

As mesenchymal stem cells (MSCs) are being investigated for regenerative therapies to be used in the clinic, delineating the roles of the IGF system in MSC growth and differentiation, in vitro, is vital in developing these cellular therapies to treat degenerative diseases. Muscle differentiation is a multistep process, starting with commitment to the muscle lineage and ending with the formation of multinucleated fibers. Insulin-like growth factor binding protein-6 (IGFBP-6), relative to other IGFBPs, has high affinity for IGF-2. However, the role of IGFBP-6 in muscle development has not been clearly defined. Our previous studies showed that in vitro extracellular IGFBP-6 increased myogenesis in early stages and could enhance the muscle differentiation process in the absence of IGF-2. In this study, we identified the signal transduction mechanisms of IGFBP-6 on muscle differentiation by placental mesenchymal stem cells (PMSCs). We showed that muscle differentiation required activation of both AKT and MAPK pathways. Interestingly, we demonstrated that IGFBP-6 could compensate for IGF-2 loss and help enhance the muscle differentiation process by triggering predominantly the MAPK pathway independent of activating either IGF-1R or the insulin receptor (IR). These findings indicate the complex interactions between IGFBP-6 and IGFs in PMSC differentiation into the skeletal muscle and that the IGF signaling axis, specifically involving IGFBP-6, is important in muscle differentiation. Moreover, although the major role of IGFBP-6 is IGF-2 inhibition, it is not necessarily the case that IGFBP-6 is the main modulator of IGF-2.

Prelamin A is involved in early steps of muscle differentiation

2008 ◽  
Vol 314 (20) ◽  
pp. 3628-3637 ◽  
Author(s):  
Cristina Capanni ◽  
Rosalba Del Coco ◽  
Stefano Squarzoni ◽  
Marta Columbaro ◽  
Elisabetta Mattioli ◽  
...  
Keyword(s):  
Muscle Differentiation ◽  
Prelamin A

scholarly journals p38 and Extracellular Signal-Regulated Kinases Regulate the Myogenic Program at Multiple Steps

2000 ◽  
Vol 20 (11) ◽  
pp. 3951-3964 ◽  
Author(s):  
Zhenguo Wu ◽  
Pamela J. Woodring ◽  
Kunjan S. Bhakta ◽  
Kumiko Tamura ◽  
Fang Wen ◽  
...  
Keyword(s):  
Muscle Differentiation ◽  
Hypertrophic Growth ◽  
Extracellular Signals ◽  
Whole Process ◽  
Extracellular Signal ◽  
Binding Factor ◽  
Mitogen Activated Protein ◽  
Activation Profile ◽  
Myogenic Program

ABSTRACT The extracellular signals which regulate the myogenic program are transduced to the nucleus by mitogen-activated protein kinases (MAPKs). We have investigated the role of two MAPKs, p38 and extracellular signal-regulated kinase (ERK), whose activities undergo significant changes during muscle differentiation. p38 is rapidly activated in myocytes induced to differentiate. This activation differs from those triggered by stress and cytokines, because it is not linked to Jun–N-terminal kinase stimulation and is maintained during the whole process of myotube formation. Moreover, p38 activation is independent of a parallel promyogenic pathway stimulated by insulin-like growth factor 1. Inhibition of p38 prevents the differentiation program in myogenic cell lines and human primary myocytes. Conversely, deliberate activation of endogenous p38 stimulates muscle differentiation even in the presence of antimyogenic cues. Much evidence indicates that p38 is an activator of MyoD: (i) p38 kinase activity is required for the expression of MyoD-responsive genes, (ii) enforced induction of p38 stimulates the transcriptional activity of a Gal4-MyoD fusion protein and allows efficient activation of chromatin-integrated reporters by MyoD, and (iii) MyoD-dependent myogenic conversion is reduced in mouse embryonic fibroblasts derived from p38α−/− embryos. Activation of p38 also enhances the transcriptional activities of myocyte enhancer binding factor 2A (MEF2A) and MEF2C by direct phosphorylation. With MEF2C, selective phosphorylation of one residue (Thr293) is a tissue-specific activating signal in differentiating myocytes. Finally, ERK shows a biphasic activation profile, with peaks of activity in undifferentiated myoblasts and postmitotic myotubes. Importantly, activation of ERK is inhibitory toward myogenic transcription in myoblasts but contributes to the activation of myogenic transcription and regulates postmitotic responses (i.e., hypertrophic growth) in myotubes.

scholarly journals The Cytoskeleton-associated PDZ-LIM Protein, ALP, Acts on Serum Response Factor Activity to Regulate Muscle Differentiation

2007 ◽  
Vol 18 (5) ◽  
pp. 1723-1733 ◽  
Author(s):  
Pascal Pomiès ◽  
Mohammad Pashmforoush ◽  
Cristina Vegezzi ◽  
Kenneth R. Chien ◽  
Charles Auffray ◽  
...  
Keyword(s):  
Serum Response Factor ◽  
Critical Role ◽  
Muscle Differentiation ◽  
Actin Dynamics ◽  
Response Factor ◽  
Cytoskeletal Regulation ◽  
Expression Construct ◽  
Filament Bundles ◽  
Serum Response

In this report, an antisense RNA strategy has allowed us to show that disruption of ALP expression affects the expression of the muscle transcription factors myogenin and MyoD, resulting in the inhibition of muscle differentiation. Introduction of a MyoD expression construct into ALP-antisense cells is sufficient to restore the capacity of the cells to differentiate, illustrating that ALP function occurs upstream of MyoD. It is known that MyoD is under the control of serum response factor (SRF), a transcriptional regulator whose activity is modulated by actin dynamics. A dramatic reduction of actin filament bundles is observed in ALP-antisense cells and treatment of these cells with the actin-stabilizing drug jasplakinolide stimulates SRF activity and restores the capacity of the cells to differentiate. Furthermore, we show that modulation of ALP expression influences SRF activity, the level of its coactivator, MAL, and muscle differentiation. Collectively, these results suggest a critical role of ALP on muscle differentiation, likely via cytoskeletal regulation of SRF.

scholarly journals Role of HuR in Skeletal Myogenesis through Coordinate Regulation of Muscle Differentiation Genes

2003 ◽  
Vol 23 (14) ◽  
pp. 4991-5004 ◽  
Author(s):  
Angélica Figueroa ◽  
Ana Cuadrado ◽  
Jinshui Fan ◽  
Ulus Atasoy ◽  
George E. Muscat ◽  
...  
Keyword(s):  
Rna Binding ◽  
Muscle Differentiation ◽  
C2c12 Cells ◽  
Dependent Manner ◽  
Skeletal Myogenesis ◽  
Critical Function ◽  
Mouse Muscle ◽  
Coordinate Regulation

ABSTRACT In this report, we investigate the role of the RNA-binding protein HuR during skeletal myogenesis. At the onset of myogenesis in differentiating C2C12 myocytes and in vivo in regenerating mouse muscle, HuR cytoplasmic abundance increased dramatically, returning to a predominantly nuclear presence upon completion of myogenesis. mRNAs encoding key regulators of myogenesis-specific transcription (myogenin and MyoD) and cell cycle withdrawal (p21), bearing AU-rich regions, were found to be targets of HuR in a differentiation-dependent manner. Accordingly, mRNA half-lives were highest during differentiation, declining when differentiation was completed. Importantly, HuR-overexpressing C2C12 cells displayed increased target mRNA expression and half-life and underwent precocious differentiation. Our findings underscore a critical function for HuR during skeletal myogenesis linked to HuR's coordinate regulation of muscle differentiation genes.

scholarly journals Sodium butyrate inhibits myogenesis by interfering with the transcriptional activation function of MyoD and myogenin.

1992 ◽  
Vol 12 (11) ◽  
pp. 5123-5130 ◽  
Author(s):  
L A Johnston ◽  
S J Tapscott ◽  
H Eisen
Keyword(s):  
Sodium Butyrate ◽  
Transcriptional Activation ◽  
Activation Function ◽  
Muscle Differentiation ◽  
Transcriptional Activators ◽  
Present Evidence ◽  
Dna Transcription ◽  
Basic Helix Loop Helix ◽  
Helix Loop Helix

Sodium butyrate reversibly inhibits muscle differentiation and blocks the expression of many muscle-specific genes in both proliferating myoblasts and differentiated myotubes. We investigated the role of the basic helix-loop-helix (bHLH) myogenic determinator proteins MyoD and myogenin in this inhibition. Our data suggest that both MyoD and myogenin are not able to function as transcriptional activators in the presence of butyrate, although both apparently retain the ability to bind DNA. Transcription of MyoD itself is extinguished in butyrate-treated myoblasts and myotubes, an effect that may be due to the inability of MyoD to autoactivate its own transcription. We present evidence that the HLH region of MyoD is essential for butyrate inhibition of MyoD. In contrast to MyoD and myogenin, butyrate does not inhibit the ubiquitous basic HLH protein E2-5 from functioning as a transcriptional activator.

Notch signalling acts in postmitotic avian myogenic cells to control MyoD activation

Development ◽  
2001 ◽  
Vol 128 (1) ◽  
pp. 107-116 ◽  
Author(s):  
E. Hirsinger ◽  
P. Malapert ◽  
J. Dubrulle ◽  
M.C. Delfini ◽  
D. Duprez ◽  
...  
Keyword(s):  
Myogenic Differentiation ◽  
Muscle Differentiation ◽  
Detailed Examination ◽  
Notch Signalling ◽  
Myogenic Cells ◽  
Myogenic Markers ◽  
Notch Activation

During Drosophila myogenesis, Notch signalling acts at multiple steps of the muscle differentiation process. In vertebrates, Notch activation has been shown to block MyoD activation and muscle differentiation in vitro, suggesting that this pathway may act to maintain the cells in an undifferentiated proliferative state. In this paper, we address the role of Notch signalling in vivo during chick myogenesis. We first demonstrate that the Notch1 receptor is expressed in postmitotic cells of the myotome and that the Notch ligands Delta1 and Serrate2 are detected in subsets of differentiating myogenic cells and are thus in position to signal to Notch1 during myogenic differentiation. We also reinvestigate the expression of MyoD and Myf5 during avian myogenesis, and observe that Myf5 is expressed earlier than MyoD, consistent with previous results in the mouse. We then show that forced expression of the Notch ligand, Delta1, during early myogenesis, using a retroviral system, has no effect on the expression of the early myogenic markers Pax3 and Myf5, but causes strong down-regulation of MyoD in infected somites. Although Delta1 overexpression results in the complete lack of differentiated muscles, detailed examination of the infected embryos shows that initial formation of a myotome is not prevented, indicating that exit from the cell cycle has not been blocked. These results suggest that Notch signalling acts in postmitotic myogenic cells to control a critical step of muscle differentiation.

Pax-3 is necessary for migration but not differentiation of limb muscle precursors in the mouse

Development ◽  
1996 ◽  
Vol 122 (3) ◽  
pp. 1017-1027 ◽  
Author(s):  
G. Daston ◽  
E. Lamar ◽  
M. Olivier ◽  
M. Goulding
Keyword(s):  
Transcription Factor ◽  
Muscle Differentiation ◽  
Precursor Cells ◽  
Limb Bud ◽  
Limb Muscle ◽  
Paired Domain ◽  
Lateral Edge ◽  
Limb Muscles ◽  
In Cells

The limb muscles of vertebrates are derived from precursor cells that migrate from the lateral edge of the dermomyotome into the limb bud. Previous studies have shown that the paired domain-containing transcription factor Pax-3 is expressed in the limb in cells that are precursors for limb muscles (Williams, B. and Ordahl, C.P. (1994) Development 120, 785–796). In splotch (Pax-3-) embryos, the limb muscles fail to develop and cells expressing Pax-3 are no longer found in the limb. In this paper we have analyzed the role of Pax-3 in the migration and subsequent differentiation of limb muscle precursors. By labeling somites adjacent to the prospective forelimb with the lipophilic dye DiI, we have shown that cells derived from these somites do not migrate into the limbs of splotch mice. The failure of limb muscle precursors to invade the limb in splotch mice is associated with the absence of c-met expression in premigratory cells, together with a change in the morphology of the ventral dermomyotome. In addition, we have shown the lateral half of somites derived from day E9.25 splotch embryos can undergo muscle differentiation when grafted into the limb bud stage 20 chick host embryos. Our results indicate that Pax-3 regulates the migration of limb muscle precursors into the limb and is not required for cells in the lateral somite to differentiate into muscle.

Sign in / Sign up

Export Citation Format

Share Document